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Article

The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met.

Nature - 14 Mar 2002

Petrelli Annalisa, Gilestro Giorgio F, Lanzardo Stefania, Comoglio Paolo M, Migone Nicola, Giordano Silvia

Abstract excerpt

Ligand-dependent downregulation of tyrosine kinase receptors is a critical step for modulating their activity. Upon ligand binding, hepatocyte growth factor (HGF) receptor (Met) is polyubiquitinated and degraded; however, the mechanisms underlying HGF receptor endocytosis are not yet known. Here...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Proto-Oncogene Proteins c-cbl

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Source

Identifiers

PMID: 11894096
DOI: 10.1038/416187a

Genes

HGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-11894096-2026-09-04.1. Manifest publication-graph-cohort-2026-09-04.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

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The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met.PMID 11894096Read ↗

Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation.Semantic proximity Read ↗

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Crk adapter proteins promote an epithelial-mesenchymal-like transition and are required for HGF-mediated cell spreading and breakdown of epithelial adherens junctions.Semantic proximity Read ↗

The basic amino acids in the coiled-coil domain of CIN85 regulate its interaction with c-Cbl and phosphatidic acid during epidermal growth factor receptor (EGFR) endocytosis.Semantic proximity Read ↗

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c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor.Semantic proximity Read ↗

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